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Manufactured by BioVendor

VCAM-1 Human HEK293 cells

  • Regulatory status:RUO
  • Type:Recombinant protein
  • Source:HEK293 cells
  • Other names:Vascular cell adhesion protein 1, CD106 antigen
  • Species:Human
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Cat. No. Size Price


RBG10340010 10 µg
RBG10340050 50 µg
RBG10340100 100 μg
PubMed Product Details
Technical Data

Type

Recombinant protein

Description

VCAM is a 110 kDa, cell surface integral membrane glycoprotein that belongs to the Ig-related superfamily of adhesion molecules. The primary function of VCAM-1 is the mediation of leukocyte-endothelial cell adhesion and signal transduction. VCAM-1 may play a vital role in the development of several diseases, including atherosclerosis and rheumatoid arthritis. The human VCAM-1 gene codes for a 715 amino acid transmembrane glycoprotein containing a 19 amino acid cytoplasmic domain, a 22 amino acid transmembrane domain, and a 674 amino acid extracellular domain. Recombinant Human VCAM-1 is a 74.1 kDa glycoprotein comprising the extracellular domain (674 amino acid residues) of VCAM-1. Monomeric glycosylated VCAM-1 migrates at an apparent molecular weight of approximately 90.0 kDa by SDS-PAGE analysis under reducing conditions.

Amino Acid Sequence

FKIETTPESRYLAQIGDSVSLTCSTTGCESPFFSWRTQIDSPLNGKVTNEGTTSTLTMNPVSFGNEHSYLCTATCESRKLEKGIQVEIYSFPKDPEIHLSGPLEAGKPITVKCSVADVYPFDRLEIDLLKGDHLMKSQEFLEDADRKSLETKSLEVTFTPVIEDIGKVLVCRAKLHIDEMDSVPTVRQAVKELQVYISPKNTVISVNPSTKLQEGGSVTMTCSSEGLPAPEIFWSKKLDNGNLQHLSGNATLTLIAMRMEDSGIYVCEGVNLIGKNRKEVELIVQEKPFTVEISPGPRIAAQIGDSVMLTCSVMGCESPSFSWRTQIDSPLSGKVRSEGTNSTLTLSPVSFENEHSYLCTVTCGHKKLEKGIQVELYSFPRDPEIEMSGGLVNGSSVTVSCKVPSVYPLDRLEIELLKGETILENIEFLEDTDMKSLENKSLEMTFIPTIEDTGKALVCQAKLHIDDMEFEPKQRQSTQTLYVNVAPRDTTVLVSPSSILEEGSSVNMTCLSQGFPAPKILWSRQLPNGELQPLSENATLTLISTKMEDSGVYLCEGINQAGRSRKEVELIIQVTPKDIKLTAFPSESVKEGDTVIISCTCGNVPETWIILKKKAETGDTVLKSIDGAYTIRKAQLKDAGVYECESKNKVGSQLRSLTLDVQGRENNKDYFSP

Source

HEK293 cells

Purity

97%

Biological Activity

Determined by its ability to support the adhesion of human U937 cells. The expected ED50 for this effect is 0.8–1.0 μg/ml.

Endotoxin

Endotoxin level is <0.1 ng/μg of protein (<1EU/μg).

Reconstitution

Centrifuge the vial prior to opening. Reconstitute in water to a concentration of 0.1–1.0 mg/ml. Do not vortex. For extended storage, it is recommended to further dilute in a buffer containing a carrier protein (example 0.1% BSA) and store in working aliquots at –20°C to –80°C.

Storage/Expiration

 –20°C

Summary

Research topic

Cell adhesion proteins

Summary

The vascular cell adhesion molecule-1 (VCAM-1) or CD106 is a member of the immunoglobulin gene superfamily. The initial molecular cloning of VCAM-1 reported six extracellular Ig-like domains (6D VCAM-1). This 6D VCAM-1 arises due to alternative splicing from a seven-domain VCAM-1 (7D VCAM-1). 7D VCAM-1 is the dominant form expressed by cultured human endothelial cells. Domains 1 through 3 are highly homologous to domains 4 through 6, suggesting that they arose by gene duplication. The cDNA of 7D VCAM-1 predicts a core protein of approximately 81 kDa with seven potential N-linked glycosylation sites. Upon complete glycosylation the mature protein has a molecular weight of approximately 102 kDa. This observation is in general agreement with immunoprecipitation studies that show a protein of approximately 110 kDa on cytokineactivated endothelium. Murine and rat VCAM-1 have been cloned. In contrast to ICAM-1, VCAM-1 appears to have been highly conserved through evolution. Both rat and mouse VCAM-1 are highly homologous at the protein level to the human VCAM-1 (77% and 76%, respectively). VCAM-1 supports the adhesion of lymphocytes, monocytes, natural killer cells, eosinophils, and basophils through its interaction with leukocyte very late antigen-4 (VLA-4). VCAM-1/VLA- 4 interaction mediates firm adherence of circulating non-neutrophilic leukocytes to endothelium. VCAM-1 also participates in leukocyte adhesion outside of the vasculature, mediating precursor lymphocyte adhesion to bone marrow stromal cells and B cell binding to lymph node follicular dendritic cells. VCAM-1 is not constitutively expressed on endothelium, but can be up-regulated in vitro in response to LPS, TNF-a, and IL-1, as well as to interferon-g and IL-4. VCAM-1 is also present on tissue macrophages, dendritic cells, bone marrow fibroblasts, myoblasts and myotubes. A soluble form of VCAM-1 (sVCAM-1) has been described. Soluble VCAM-1 levels have been found in the serum of healthy individuals and increased levels of sVCAM-1 can be detected in several diseases.

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